Description
The ∆-4,5-Glycuronidase acts on the non-sulphated, unsaturated termini of disaccharides, tetrasaccharides, etc., produced either directly by lyase action on a glycosaminoglycan or by the action of the 2-O-sulphatase on an unsaturated disaccharide, tetrasaccharide, etc.
Source
Flavobacterium heparinum (ATCC 13125)
Form
The enzyme is stabilised with 0.2% BSA, 0.22 um sterile-filtered and dispensed into sterile vials. To preserve high activity, the enzyme solution is stored frozen at -60°C and is supplied world-wide as a frozen solution.
Enzyme Commission Number
EC 3.2.1-
Contaminants
NMT 0.1% (nominally)
Specificity
The enzyme is one of two ‘secondary’ enzymes (the other being 2-O-sulphatase) involved in the degradation of glycosaminoglycans by the Flavobacterium enzyme consortium. In combination with 2-O-sulphatase, they are used to characterise heparin fragments after treatment with heparinase. The two enzymes attack the unsaturated disaccharides and oligosaccharides produced from glycosaminoglycans by the lyases, the 'primary' enzymes. The two enzymes work in strict sequence to raze the terminal, 2-O-sulphated unsaturated moiety from disaccharides, tetrasaccharides, etc. The 2-O-sulphatase operates first, followed by the ∆-4,5-glycuronidase, to produce a hexosamine monosaccharide from a disaccharide, or an oddnumbered oligosaccharide from an even-numbered oligosaccharide.
Unit Definition
One unit will form 1 micromole of hydrolysed product (monosaccharide and keto-acid) per minute at pH 7.0 at 25°C using heparin unsaturated disaccharide IV-A (GEH1008) as substrate.
Storage
Store frozen at -20 or below upon receipt. Avoid repeated freezethawing.
Synonyms
∆-4,5–Glycuronidase; Glycuronidase